ID NAGK_ECOUT Reviewed; 303 AA. AC Q1RD35; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=N-acetyl-D-glucosamine kinase; DE EC=2.7.1.59; DE AltName: Full=GlcNAc kinase; GN Name=nagK; OrderedLocusNames=UTI89_C1247; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine CC (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P CC (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl- CC D-glucosamine 6-phosphate. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC -!- SIMILARITY: Belongs to the ROK (nagC/xylR) family. NagK subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE06729.1; -; Genomic_DNA. DR RefSeq; YP_540260.1; -. DR SMR; Q1RD35; 1-303. DR GeneID; 3992705; -. DR GenomeReviews; CP000243_GR; UTI89_C1247. DR KEGG; eci:UTI89_C1247; -. DR HOGENOM; Q1RD35; -. DR OMA; Q1RD35; HVERFME. DR BioCyc; ECOL364106:UTI89_C1247-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:HAMAP. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:HAMAP. DR HAMAP; MF_01271; -; 1. DR InterPro; IPR000600; ROK. DR Pfam; PF00480; ROK; 1. DR PROSITE; PS01125; ROK; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Metal-binding; Nucleotide-binding; Transferase; Zinc. FT CHAIN 1 303 N-acetyl-D-glucosamine kinase. FT /FTId=PRO_0000270104. FT NP_BIND 4 11 ATP (Potential). FT NP_BIND 133 140 ATP (Potential). FT METAL 157 157 Zinc (By similarity). FT METAL 177 177 Zinc (By similarity). FT METAL 179 179 Zinc (By similarity). FT METAL 184 184 Zinc (By similarity). SQ SEQUENCE 303 AA; 33085 MW; 0757E639EB22510C CRC64; MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DRRFGCKGSV GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT QYPLVMGLIL GTGVGGGLIF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG QHGCIENYLS GRGFAWLYQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI LTIVDPDLVV IGGGLSNFPA ITTQLAERLP RHLLPVARVP RIERARHGDA GGMRGAAFLH LTD //